ID NDUV3_HUMAN Reviewed; 108 AA. AC P56181; A8K0M1; J3KNX7; Q6FGD3; Q8WU60; Q9HCR5; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2002, sequence version 2. DT 16-SEP-2015, entry version 123. DE RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial; DE AltName: Full=Complex I-9kD; DE Short=CI-9kD; DE AltName: Full=NADH-ubiquinone oxidoreductase 9 kDa subunit; DE AltName: Full=Renal carcinoma antigen NY-REN-4; DE Flags: Precursor; GN Name=NDUFV3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9344673; DOI=10.1006/geno.1997.4930; RA de Coo R.F.M., Buddiger P., Smeets H.J.M., van Oost B.A.; RT "Molecular cloning and characterization of the human mitochondrial RT NADH:oxidoreductase 10-kDa gene (NDUFV3)."; RL Genomics 45:434-437(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10950923; DOI=10.1006/geno.2000.6253; RA Berry A., Scott H.S., Kudoh J., Talior I., Korostishevsky M., RA Wattenhofer M., Guipponi M., Barras C., Rossier C., Shibuya K., RA Wang J., Kawasaki K., Asakawa S., Minoshima S., Shimizu N., RA Antonarakis S.E., Bonne-Tamir B.; RT "Refined localization of autosomal recessive nonsyndromic deafness RT DFNB10 locus using 34 novel microsatellite markers, genomic structure, RT and exclusion of six known genes in the region."; RL Genomics 68:22-29(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., RA Korn B., Zuo D., Hu Y., LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cerebellum; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10830953; DOI=10.1038/35012518; RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., RA Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., RA Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., RA Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., RA Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., RA Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., RA Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., RA Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., RA Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., RA Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., RA Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., RA Lehrach H., Reinhardt R., Yaspo M.-L.; RT "The DNA sequence of human chromosome 21."; RL Nature 405:311-319(2000). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP IDENTIFICATION AS A RENAL CANCER ANTIGEN. RC TISSUE=Renal cell carcinoma; RX PubMed=10508479; RX DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5; RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., RA Old L.J.; RT "Antigens recognized by autologous antibody in patients with renal- RT cell carcinoma."; RL Int. J. Cancer 83:456-464(1999). RN [9] RP IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=12611891; DOI=10.1074/jbc.C300064200; RA Murray J., Zhang B., Taylor S.W., Oglesbee D., Fahy E., Marusich M.F., RA Ghosh S.S., Capaldi R.A.; RT "The subunit composition of the human NADH dehydrogenase obtained by RT rapid one-step immunopurification."; RL J. Biol. Chem. 278:13619-13622(2003). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-162 AND SER-164 RP (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 AND SER-164 (ISOFORM RP 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Accessory subunit of the mitochondrial membrane CC respiratory chain NADH dehydrogenase (Complex I), that is believed CC not to be involved in catalysis. Complex I functions in the CC transfer of electrons from NADH to the respiratory chain. The CC immediate electron acceptor for the enzyme is believed to be CC ubiquinone. CC -!- SUBUNIT: Complex I is composed of 45 different subunits. This is a CC component of the flavoprotein-sulfur (FP) fragment of the enzyme. CC {ECO:0000269|PubMed:12611891}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral CC membrane protein; Matrix side. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P56181-1; Sequence=Displayed; CC Name=2; CC IsoId=P56181-2; Sequence=VSP_038552; CC Note=Ref.7 (AAH21217) sequence is in conflict in position: CC 415:D->N. Contains a phosphoserine at position 164. Contains a CC phosphoserine at position 160. Contains a phosphoserine at CC position 162. {ECO:0000244|PubMed:18669648, CC ECO:0000244|PubMed:24275569, ECO:0000305}; CC -!- SIMILARITY: Belongs to the complex I NDUFV3 subunit family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X99726; CAB56704.1; -; Genomic_DNA. DR EMBL; X99727; CAB56704.1; JOINED; Genomic_DNA. DR EMBL; X99728; CAB56704.1; JOINED; Genomic_DNA. DR EMBL; AB038163; BAB13732.1; -; Genomic_DNA. DR EMBL; CR542174; CAG46971.1; -; mRNA. DR EMBL; CR542190; CAG46987.1; -; mRNA. DR EMBL; AK289586; BAF82275.1; -; mRNA. DR EMBL; AP001629; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471079; EAX09524.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09526.1; -; Genomic_DNA. DR EMBL; BC021217; AAH21217.2; -; mRNA. DR EMBL; BC033766; AAH33766.1; -; mRNA. DR EMBL; BC054016; AAH54016.1; -; mRNA. DR CCDS; CCDS33572.1; -. [P56181-2] DR CCDS; CCDS33573.1; -. [P56181-1] DR RefSeq; NP_001001503.1; NM_001001503.1. [P56181-1] DR RefSeq; NP_066553.3; NM_021075.3. [P56181-2] DR UniGene; Hs.473937; -. DR ProteinModelPortal; P56181; -. DR BioGrid; 110809; 21. DR IntAct; P56181; 12. DR MINT; MINT-4535662; -. DR STRING; 9606.ENSP00000346196; -. DR ChEMBL; CHEMBL2363065; -. DR PhosphoSite; P56181; -. DR BioMuta; NDUFV3; -. DR MaxQB; P56181; -. DR PaxDb; P56181; -. DR PRIDE; P56181; -. DR DNASU; 4731; -. DR Ensembl; ENST00000340344; ENSP00000342895; ENSG00000160194. [P56181-1] DR Ensembl; ENST00000354250; ENSP00000346196; ENSG00000160194. [P56181-2] DR GeneID; 4731; -. DR KEGG; hsa:4731; -. DR UCSC; uc002zcm.3; human. DR UCSC; uc002zcn.3; human. [P56181-1] DR CTD; 4731; -. DR GeneCards; GC21P042879; -. DR HGNC; HGNC:7719; NDUFV3. DR HPA; CAB034142; -. DR HPA; HPA019791; -. DR HPA; HPA020463; -. DR HPA; HPA030427; -. DR MIM; 602184; gene. DR neXtProt; NX_P56181; -. DR PharmGKB; PA31529; -. DR eggNOG; NOG47709; -. DR GeneTree; ENSGT00390000012196; -. DR HOGENOM; HOG000013001; -. DR HOVERGEN; HBG082013; -. DR InParanoid; P56181; -. DR KO; K03944; -. DR OMA; SQKPFEV; -. DR OrthoDB; EOG7QZGCS; -. DR PhylomeDB; P56181; -. DR TreeFam; TF338771; -. DR Reactome; R-HSA-611105; Respiratory electron transport. DR ChiTaRS; NDUFV3; human. DR GeneWiki; NDUFV3; -. DR GenomeRNAi; 4731; -. DR NextBio; 18240; -. DR PRO; PR:P56181; -. DR Proteomes; UP000005640; Chromosome 21. DR Bgee; P56181; -. DR CleanEx; HS_NDUFV3; -. DR Genevisible; P56181; HS. DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome. DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; NAS:UniProtKB. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0044237; P:cellular metabolic process; TAS:Reactome. DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; NAS:UniProtKB. DR GO; GO:0022904; P:respiratory electron transport chain; TAS:Reactome. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR InterPro; IPR026193; NDUFV3. DR PANTHER; PTHR17117; PTHR17117; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Electron transport; Membrane; KW Mitochondrion; Mitochondrion inner membrane; Phosphoprotein; KW Reference proteome; Respiratory chain; Transit peptide; Transport. FT TRANSIT 1 34 Mitochondrion. {ECO:0000250}. FT CHAIN 35 108 NADH dehydrogenase [ubiquinone] FT flavoprotein 3, mitochondrial. FT /FTId=PRO_0000020025. FT VAR_SEQ 56 57 KK -> KNVVEPKERGKLLATQTAAELSKNLSSPSSYPPAV FT NKGRKVASPSPSGSVLFTDEGVPKFLSRKTLVEFPQKVLSP FT FRKQGSDSEARQVGRKVTSPSSSSSSSSSDSESDDEADVSE FT VTPRVVSKGRGGLRKPEASHSFENRAPRVTVSAKEKTLLQK FT PHVDITDPEKPHQPKKKGSPAKPSEGRENARPKTTMPRSQV FT DEEFLKQSLKEKQLQKTFRLNEIDKESQKPFEVKGPLPVHT FT KSGLSAPPKGSPAPAVLAEEARAEGQLQASPPGAAEGHLEK FT PVPEPQRKAAPPLPRKETSGTQGIEGHLKGGQAIVEDQIPP FT SNLETVPVENNHGFHEKTAALKLEAEGEAMEDAAAPGDDRG FT GTQE (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_038552. FT CONFLICT 9 9 Q -> K (in Ref. 1; CAB56704). FT {ECO:0000305}. SQ SEQUENCE 108 AA; 11941 MW; BD7375474AB0B1EC CRC64; MAAPCLLRQG RAGALKTMLQ EAQVFRGLAS TVSLSAESGK SEKGQPQNSK KQSPPKKPAP VPAEPFDNTT YKNLQHHDYS TYTFLDLNLE LSKFRMPQPS SGRESPRH //